Plasma membrane phospholipid signature recruits the plant exocyst complex via the EX070A1 subunit
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F21%3A10432704" target="_blank" >RIV/00216208:11310/21:10432704 - isvavai.cz</a>
Result on the web
<a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=i3ST0s8fuh" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=i3ST0s8fuh</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1073/pnas.2105287118" target="_blank" >10.1073/pnas.2105287118</a>
Alternative languages
Result language
angličtina
Original language name
Plasma membrane phospholipid signature recruits the plant exocyst complex via the EX070A1 subunit
Original language description
Polarized exocytosis is essential for many vital processes in eukaryotic cells, where secretory vesicles are targeted to distinct plasma membrane domains characterized by their specific lipid-protein composition. Heterooctameric protein complex exocyst facilitates the vesicle tethering to a target membrane and is a principal cell polarity regulator in eukaryotes. The architecture and molecular details of plant exocyst and its membrane recruitment have remained elusive. Here, we show that the plant exocyst consists of two modules formed by SEC3-SEC5-SEC6-SEC8 and SEC10-SEC15-EX070EX084 subunits, respectively, documenting the evolutionarily conserved architecture within eukaryotes. In contrast to yeast and mammals, the two modules are linked by a plant-specific SEC3EX070 interaction, and plant EX070 functionally dominates over SEC3 in the exocyst recruitment to the plasma membrane. Using an interdisciplinary approach, we found that the C-terminal part of EX070A1, the canonical EX070 isoform in Arabidopsis, is critical for this process. In contrast to yeast and animal cells, the EX070A1 interaction with the plasma membrane is mediated by multiple anionic phospholipids uniquely contributing to the plant plasma membrane identity. We identified several evolutionary conserved EX070 lysine residues and experimentally proved their importance for the EX070A1-phospholipid interactions. Collectively, our work has uncovered plant-specific features of the exocyst complex and emphasized the importance of the specific protein-lipid code for the recruitment of peripheral membrane proteins.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10611 - Plant sciences, botany
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Proceedings of the National Academy of Sciences of the United States of America
ISSN
0027-8424
e-ISSN
1091-6490
Volume of the periodical
118
Issue of the periodical within the volume
36
Country of publishing house
US - UNITED STATES
Number of pages
12
Pages from-to
e2105287118
UT code for WoS article
000694705600001
EID of the result in the Scopus database
2-s2.0-85114132837